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L723P

Category 3/4 — Most DruggablePathogenicLumenal · predictedσ-1 candidateEditorial
LeucineProline at position 723 · C-terminal lumenal domain (653-869) · WFS1 (Wolframin)

Leucine → Proline at position 723 in wolframin's C-terminal lumenal domain. ClinVar Pathogenic. AlphaMissense 0.959, DynaMut2 ΔΔG -0.19 kcal/mol (destabilising). Another proline-introduction variant in the lumenal fold.

Interactive 3D Structure

Wild-type reference
Wild-type L723 — hydrogen bond to I720
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DynaMut2 mutant · L723P
Mutant P723 — hydrogen bond to I720 lost (2 contacts lost)
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Bond changes · DynaMut2 interaction analysis

2 lost2 gained3 preserved
Interaction typeWild-type partnerMutant partnerStatus
Hydrogen bondI720I720Preserved
Polar contactA719Gained
Polar contactI720I720Preserved
Van der WaalsI720Gained
Van der WaalsN721Lost
HydrophobicI727I727Preserved
HydrophobicM731Lost

Lost / gained / preserved interatomic contacts at the variant residue, from the DynaMut2 (Arpeggio) interaction analysis of the wild-type and energy-minimized mutant structures.

Computational Predictions

DynaMut2 ΔΔG
-0.19kcal/mol
Destabilising — mild
AlphaMissense
0.959
LPath
AlphaFold pLDDT
83
model confidence
Schema
Cat 3/4
Category 3/4 — Most Druggable

Clinical Evidence

ClinVar classificationPathogenic
Review statuscriteria provided, single submitter
Associated conditions(no specific conditions catalogued for L723P — ClinVar Pathogenic by review evidence)
InheritanceInheritance not specified. ClinVar Pathogenic.
Population frequency (gnomAD v4)Absent from gnomAD v4
cDNA changec.2168T>C
ClinVar accessionVCV002203530
Last evaluated2024/12/16 00:00

Not observed in ~730k individuals — consistent with a rare allele (ACMG PM2_supporting).

Structural Context

Position 723 sits in wolframin's C-terminal lumenal domain. The AlphaFold model places L723 within 5 Å of MET722 (2.5 Å), PRO724 (2.5 Å), ILE720 (3.6 Å), ASN721 (4.6 Å), and ALA719 (4.8 Å). The local environment is hydrophobic-rich (M722, I720, A719) with a single polar residue (N721). Notably, PRO724 sits at 2.5 Å — the immediate downstream neighbor is already a proline.

Replacing L723 with proline introduces a second proline immediately adjacent to the existing P724 — a Pro-Pro motif is unusual and structurally distinctive. Two adjacent prolines create a particularly rigid backbone segment with restricted conformational options. The wild-type Leu-Pro motif at 723-724 transitions from flexible to constrained backbone; the variant Pro-Pro motif is constrained on both sides.

The |ΔΔG| of 0.19 is modest — the fold absorbs the new proline because the local environment was already constrained. But the geometry shifts: the Pro-Pro motif likely adopts a different local conformation than the wild-type Leu-Pro, and surrounding residues (M722, I720) rearrange to accommodate.

AlphaMissense's 0.959 score captures the functional severity — the shifted local geometry disrupts whatever interaction the wild-type Leu-Pro motif enabled.

Amino-acid chemistry
Leucine (L) → Proline (P) — flexible branched hydrophobic replaced by rigid helix-breaking residue. Same proline-introduction mechanism class as L543P, L402P, L804P.
Position in the protein
C-terminal lumenal domain · position 723 in the ER lumen (pLDDT 83).

Druggability Assessment

Category 3/4 — Most Druggable. |ΔΔG| = 0.19 kcal/mol — fold essentially unperturbed. AlphaMissense 0.959 confirms pathogenic mechanism is functional rather than structural.

The mechanism is creation of an unusual Pro-Pro motif at positions 723-724, shifting the local backbone geometry from a Leu-Pro transition to a rigid Pro-Pro segment. Therapeutic strategy: site-directed small molecules at the position 720-724 region, ideally compensating for the geometric shift.

This is one of several proline-introduction variants in the Atlas (L402P, L543P, L723P, L804P). The therapeutic vocabulary across this class is consistent: stabilize local backbone geometry against the introduced proline kink.

Why this matters

L723P creates a Pro-Pro motif rare in folded proteins. The Atlas's neighbor analysis surfaces this directly — PRO724 at 2.5 Å is the next-residue neighbor. The unusual geometry of two adjacent prolines is what distinguishes L723P's mechanism from other proline-introduction variants in the Atlas.
Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the L723P PDF below and upload it to Wolfram Intelligence to generate therapeutic-strategy proposals — guanidinium mimetics, sigma-1 agonist docking, NAC thiol-capping. NAC is already on the bench-testing list.

Download L723P PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.

UniProt Domain Annotation

Chain1890 · Wolframin
Topological domain653869 · Lumenal